1pd2
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene> | |LIGAND= <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Prostaglandin-D_synthase Prostaglandin-D synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.99.2 5.3.99.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Prostaglandin-D_synthase Prostaglandin-D synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.99.2 5.3.99.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pd2 OCA], [http://www.ebi.ac.uk/pdbsum/1pd2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pd2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ago, H.]] | [[Category: Ago, H.]] | ||
[[Category: Miyano, M.]] | [[Category: Miyano, M.]] | ||
| - | [[Category: GTT]] | ||
[[Category: gst]] | [[Category: gst]] | ||
[[Category: hematopoietic prostaglandin d synthase]] | [[Category: hematopoietic prostaglandin d synthase]] | ||
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[[Category: sigma-class gst]] | [[Category: sigma-class gst]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:58:03 2008'' |
Revision as of 19:58, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Prostaglandin-D synthase, with EC number 5.3.99.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE
Overview
Hematopoietic prostaglandin (PG) D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells. We isolated a cDNA for the rat enzyme, crystallized the recombinant enzyme, and determined the three-dimensional structure of the enzyme complexed with glutathione at 2.3 A resolution. The enzyme is the first member of the sigma class glutathione S-transferase (GST) from vertebrates and possesses a prominent cleft as the active site, which is never seen among other members of the GST family. The unique 3-D architecture of the cleft leads to the putative substrate binding mode and its catalytic mechanism, responsible for the specific isomerization from PGH2 to PGD2.
About this Structure
1PD2 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Cloning and crystal structure of hematopoietic prostaglandin D synthase., Kanaoka Y, Ago H, Inagaki E, Nanayama T, Miyano M, Kikuno R, Fujii Y, Eguchi N, Toh H, Urade Y, Hayaishi O, Cell. 1997 Sep 19;90(6):1085-95. PMID:9323136
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